C3114
Anti-Calpain-13 (Domain III, N-Terminal), Large Subunit antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution
生物来源
rabbit
质量水平
偶联物
unconjugated
抗体形式
affinity isolated antibody
抗体产品类型
primary antibodies
克隆
polyclonal
表单
buffered aqueous glycerol solution
种属反应性
rat, human, mouse
浓度
~1 mg/mL
技术
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
western blot: 1:1,000
UniProt登记号
运输
wet ice
储存温度
−20°C
基因信息
human ... CAPN13(92291)
mouse ... Capn13(381122)
rat ... Capn13(362701)
一般描述
Calpains are calcium-activated, non-lysosomal cysteine proteases that cleave cytoskeletal and submembranous proteins. It is an intracellular cysteine protease that is present in all mammalian tissues. Anti-Calpain-13 (Domain I, N-Terminal), Large Subunit is developed in rabbit using a synthetic peptide corresponding to domain I of the large subunit of human calpain 13 (capn-13) as immunogen. The antibody is affinity purified using agarose to which the immunogen peptide has been bound.
免疫原
synthetic peptide corresponding to domain III of the large subunit of human calpain 13.
应用
Anti-Calpain-13 is suitable for immunohistochemistry, immunoprecipitation and indirect ELISA. It is also suitable for western blot at a dilution of 1:1,000
生化/生理作用
Calpains are involved in a variety of processes including cytoskeletal reorganization, muscle protein degradation, cell proliferation, differentiation, and vesicular secretion. Anti-Calpain-13 (Domain I, N-Terminal), Large Subunit recognizes domain I in the large subunit of human calpain 13 by various immunochemical techniques including immunoblotting, immunoprecipitation, immunohistochemistry, and ELISA. It detects human, rat, and mouse calpain 13 and does not crossreact with other calpain family members (calpain 1, calpain 2, calpain 3, etc.). The antibody binds to the reduced and non-reduced protein. By immunoblotting against the reduced protein, the antibody identifies bands at approximately 64 kDa, 52 kDa, 48 kDa, 40 kDa, and aseries of smaller forms.
外形
Solution in 0.01 M phosphate buffered saline containing 50% glycerol and 0.05% sodium azide.
免责声明
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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储存分类代码
10 - Combustible liquids
法规信息
新产品
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D Stockholm et al.
Experimental cell research, 252(2), 392-400 (1999-10-21)
We have synthesized dextran derivatives called RGTAs (for regenerating agents) that were designed to mimic some of the properties of heparin or heparan sulfate to interact with and protect heparin binding growth factors. Some of these growth factors have been
S Kulkarni et al.
The Journal of biological chemistry, 274(30), 21265-21275 (1999-07-20)
Integrin-induced adhesion leads to cytoskeletal reorganizations, cell migration, spreading, proliferation, and differentiation. The details of the signaling events that induce these changes in cell behavior are not well understood but they appear to involve activation of Rho family members which
S S Murray et al.
Experimental cell research, 233(2), 297-309 (1997-06-15)
The calpain-calpastatin system, which consists of calpains I and II (two ubiquitously distributed calcium-activated papain-like cysteine proteases), as well as calpastatin (the endogenous calpain inhibitor), plays an important role in cell proliferation and differentiation in many tissues. However, its contribution
D Balcerzak et al.
Journal of cell science, 108 ( Pt 5), 2077-2082 (1995-05-01)
Previous studies have led to the hypothesis of a possible role for m-calpain (EC 3.4.22.17) in myoblast fusion in culture in vitro. To support this hypothesis, an antisense strategy has been used with cultured primary rat myoblasts. Using an appropriate
G V Johnson et al.
BioEssays : news and reviews in molecular, cellular and developmental biology, 19(11), 1011-1018 (1997-12-12)
Calpains are a family of calcium-dependent thiol-proteases which are proposed to be involved in many physiological processes as well as pathological conditions. Calpains are likely to be involved in processing of numerous enzymes and cytoskeletal components, thereby linking their activity
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